Sialic acids are negatively charged nine carbon monosaccharides located terminally on glycoproteins and glycolipids that control cellular physiological processes. Sialylation is a post translational modification (ptm) regulated by enzymes and has been studied in prokaryotes including bacteria, dueterostomes including vertebrates, Cephalochordates, Ascidians, Echinoderms and protostomes including Molluscs and Arthropods and Plant. Although diverse structures of sialylated molecules have been reported in different organisms, unravelling sialylation in insect biology is a completely new domain. Within protostomes, the study of sialylation in members of Phylum Arthropoda and Class Insecta finds importance. Reports on sialylation in some insects exist. Genetically engineered components of sialylation pathway in Spodoptera frugiperda (Sf9) cell lines have enabled our understanding of sialylation and expression of mammalian proteins in insects. In this study we have summarised the finding on (i) sialylated molecules (ii) processes and enzymes involved (iii) function of sialylation (iv) genetic engineering approaches and generation of mammalian protein expression systems (v) a comparison of sialylation machinery in insects with that of mammals (vi) genes and transcriptional regulation in insects. At present no information on structural studies of insect sialyltransferase (STs) exist. We report minor differences in ST structure in insects on complete protein sequences recorded in Genbank through in silico approaches. An indepth study of all the components of the sialylation pathway in different insect species across different families and their evolutionary significance finds importance as the future scope of this review.
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http://dx.doi.org/10.1007/s10719-018-9835-6 | DOI Listing |
ACS Omega
December 2024
Laboratorio de Glicobiología y Diagnóstico Molecular, Centro de Investigación en Dinámica Celular, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, Cuernavaca 62209, Morelos, México.
The human CMP-sialic acid transporter (hCST) is a mammalian highly conserved type III antiporter that translocates CMP-sialic acid into the Golgi lumen, supporting sialylation. Although different works have focused on elucidating structure-function relationships in the hCST, this is the first study to address them in an alternatively spliced isoform. We have previously reported the expression of a functional human del177 isoform that has skipping of exon 6, resulting in a loss of 59 amino acids, without change in the open reading frame and conserving its C-terminal region.
View Article and Find Full Text PDFBiotechnol Bioeng
December 2024
Department of Chemical and Biomolecular Engineering, University of Delaware, Newark, Delaware, USA.
The CHO VRC01 cell line produces an anti-HIV IgG1 monoclonal antibody containing N-linked glycans on both the Fab (variable) and Fc (constant) regions. Site-specific glycan analysis was used to measure the complex effects of cell culture process conditions on Fab and Fc glycosylation. Experimental data revealed major differences in glycan fractions across the two sites.
View Article and Find Full Text PDFSci Rep
December 2024
Leiden University Center for Infectious Diseases (LUCID), Leiden University Medical Center (LUMC), Albinusdreef 2, 2333ZA, Leiden, Zuid-Holland, The Netherlands.
Antibody glycosylation patterns can affect antibody functionality and thereby contribute to protection against invading pathogens. During pregnancy, maternal antibodies can be transferred through the placenta and contribute to modulating both the mother's and her child's immune responses. Although several studies of IgG glycosylation during pregnancy have been carried out, very few cohorts studied were from sub-Saharan Africa, where exposure to microorganisms and parasites is high.
View Article and Find Full Text PDFSpectrochim Acta A Mol Biomol Spectrosc
December 2024
Department of Chemistry, Indian Institute of Technology Roorkee, Roorkee 247667, Uttarakhand, India. Electronic address:
Sialic acid, a negatively charged nine-carbon monosaccharide, is mainly located at the terminal end of glycan chains on glycoproteins and glycolipids of cell surface and most secreted proteins. Elevated levels of sialylated glycans have been known as a hallmark in numerous cancers. As a result, sialic acid acts as a useful and accessible cancer biomarker for early cancer detection and monitoring the disease development during cancer treatment which is crucial in elevating the survival rate.
View Article and Find Full Text PDFFood Chem
December 2024
Chinese Academy of Inspection and Quarantine, Beijing 100176, People's Republic of China. Electronic address:
Glycoproteins, which are involved in numerous biological functions, are among the most critical functional ingredients in an edible bird's nest (EBN). To gain a comprehensive understanding of the glycoprotein species within EBN, a label-free, site-specific glycoproteomic approach was used to analyze their N-glycoproteins, N-glycopeptides, and N-glycans systematically. A total of 127 N-glycoproteins were identified in EBN, of which 72 were found in house-EBN and 63 in cave-EBN, yielding 4195 and 5649 glycopeptides, respectively.
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